ID   MOG_HELPY               Reviewed;         176 AA.
AC   P56421;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Molybdopterin adenylyltransferase;
DE            Short=MPT adenylyltransferase;
DE            EC=2.7.7.75;
GN   Name=mog; Synonyms=mogA; OrderedLocusNames=HP_0799;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
CC   -!- FUNCTION: Catalyzes the adenylation of molybdopterin as part of the
CC       biosynthesis of the molybdenum-cofactor. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + molybdopterin = adenylyl-molybdopterin +
CC         diphosphate; Xref=Rhea:RHEA:31331, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58698,
CC         ChEBI:CHEBI:62727; EC=2.7.7.75;
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC   -!- SIMILARITY: Belongs to the MoaB/Mog family. {ECO:0000305}.
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DR   EMBL; AE000511; AAD07849.1; -; Genomic_DNA.
DR   PIR; G64619; G64619.
DR   RefSeq; NP_207592.1; NC_000915.1.
DR   RefSeq; WP_001193328.1; NC_018939.1.
DR   AlphaFoldDB; P56421; -.
DR   SMR; P56421; -.
DR   IntAct; P56421; 2.
DR   STRING; 85962.C694_04095; -.
DR   PaxDb; P56421; -.
DR   EnsemblBacteria; AAD07849; AAD07849; HP_0799.
DR   KEGG; hpy:HP_0799; -.
DR   PATRIC; fig|85962.47.peg.851; -.
DR   eggNOG; COG0521; Bacteria.
DR   OMA; EYLTSEW; -.
DR   PhylomeDB; P56421; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00886; MogA_MoaB; 1.
DR   Gene3D; 3.40.980.10; -; 1.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR008284; MoCF_biosynth_CS.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; SSF53218; 1.
DR   TIGRFAMs; TIGR00177; molyb_syn; 1.
DR   PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..176
FT                   /note="Molybdopterin adenylyltransferase"
FT                   /id="PRO_0000170985"
SQ   SEQUENCE   176 AA;  19677 MW;  9E244CC047172703 CRC64;
     MQTIHIGVLS ASDRASKGIY EDLSGKAIQE VLSEYLLNPL EFYYEIVADE RDLIEKSLIK
     MCDEYQCDLV VTTGGTGPAL RDITPEATEK VCQKMLPGFG ELMRMTSLKY VPTAILSRQS
     AGIRNKSLII NLPGKPKSIR ECLEAVFPAI PYCVDLILGN YMQVNEKNIQ AFRPKQ